| 马面鱼皮胶原抗氧化肽的分离制备及稳定性研究 |
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| 引用本文： | 蔡金秀,夏姗姗,马佳雯,王佳圆,杨华,曹少谦,戚向阳.马面鱼皮胶原抗氧化肽的分离制备及稳定性研究[J].核农学报,2021,35(11):2569-2577. |
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| 作者姓名： | 蔡金秀 夏姗姗 马佳雯 王佳圆 杨华 曹少谦 戚向阳 |
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| 作者单位： | 1上海海洋大学食品学院,上海 2013062浙江万里学院生物与环境学院,浙江 宁波 315100 |
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| 基金项目： | 浙江省重点研发项目(2019C02071);十三五海洋经济创新发展示范项目(NBHY-2017-S2);浙江省一流学科“生物工程”学生创新项目(CX2019001) |
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| 摘 要： | 为促进对马面鱼皮资源的综合利用,开发高附加值产品,本试验以DPPH自由基清除率和水解度(DH)为评价指标,探讨马面鱼皮胶原蛋白的最佳酶解工艺,并采用超滤和凝胶柱层析法分离制备抗氧化肽,通过超高效液相色谱-质谱联用(UPLC-MS)法对其进行结构解析。此外,还探讨了pH值、温度及体外模拟消化对多肽抗氧化活性的影响。结果表明,利用双酶分步酶解法可制备高活性抗氧化多肽,即在底物浓度3%,加酶量3 600 U·g-1以及温度50℃的条件下先用Proteasea A ‘Amano’2G酶解3 h,再用酸性蛋白酶酶解2 h,清除DPPH自由基的IC50值为13.03 mg·mL -1。经超滤及柱层析分离后,可得到抗氧化活性较高的A1组分,其清除DPPH自由基的 IC50值为1.80 mg·mL-1。稳定性研究结果表明,所制备的胶原蛋白抗氧化肽热稳定性好,在偏酸性条件下能保持较高的活性,经体外模拟胃肠消化后仍能保持较高的抗氧化活性。根据UPLC-MS分析推测A1的氨基酸序列可能为Gly-Glu-Gly-Ala-Cys-Asn或Asn-Glu-Gly-Ala-Cys-Gly。本研究结果为马面鱼皮的高值化利用及高活性抗氧化肽的筛选提供了一定的理论依据。
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| 关 键 词： | 胶原蛋白 抗氧化肽 分离 稳定性 |
| 收稿时间： | 2020-09-15 |
Isolation,Preparation and Stability of Collagen Antioxidant Peptides From the Skin of Navodon Septentrionalis |
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| CAI Jinxiu,XIA Shanshan,MA Jiawen,WANG Jiayuan,YANG Hua,CAO Shaoqian,QI Xiangyang.Isolation,Preparation and Stability of Collagen Antioxidant Peptides From the Skin of Navodon Septentrionalis[J].Acta Agriculturae Nucleatae Sinica,2021,35(11):2569-2577. |
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| Authors: | CAI Jinxiu XIA Shanshan MA Jiawen WANG Jiayuan YANG Hua CAO Shaoqian QI Xiangyang |
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| Institution: | 1College of Food Science and Technology, Shanghai Ocean University, Shanghai 2013062College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo, Zhejiang 315100 |
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| Abstract: | In order to improve the comprehensive utilization of navodon septentrionalis skin, and develop high value-added products, DPPH scavenging rate and hydrolysis degree (DH) were used as the evaluation indexes to investigate the optimum enzymatic hydrolysis conditions of collagen from the skin of navodon septentrionalis. The collagen antionxidant peptides were purified by ultrafiltration and gel filtration chromatography, and Ultra Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS) was used to analyze the structure. In addition, we also investigated the effect of pH, temperature and gastrointestinal-digestion on the antionxidant peptides. The results revealed that high-activity antioxidant peptide could be obtained using the two-step enzymatic hydrolysis. The optimal enzymatic hydrolysis conditions were substrate concentration of 3%, enzyme dosage of 3 600 U·g-1, hydrolysis temperature of 50℃, hydrolysis with the proteasea A “Amano”2G for 3 hours, and further hydrolyzed for 2 hours with acid protease. Under hydrolysis prosess, the ·DPPH scavenging IC50 value of the hydrolysate was 13.03 mg·mL -1. The A1 fraction with high antioxidant activity was obtained by ultrafiltration and gel filtration chromatography, the ·DPPH scavenging IC50 value of which was 1.8 mg·mL -1. The stability study showed that the prepared collagen antioxidant peptide exhibit sound thermal stability, which could maintain high activity under the acidic condition, as well as good stability in in vitro system by simulating gastrointestinal digestion. UPLC-MS analysis speculated that the amino acid sequence of A1 might be Gly-Glu-Gly-Ala-Cys-Asn or Asn-Glu-Gly-Ala-Cys-Gly. The results provide a theoretical basis for the high-value utilization of skin of navodon septentrionalis and the screening of high-activity antioxidant peptides |
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| Keywords: | collagen antioxidant peptides purification stability |
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